Evidence map›Paper›PMID 24369724›Full record

ArticleJournal of proteome research2014

Enhanced identification of zero-length chemical cross-links using label-free quantitation and high-resolution fragment ion spectra.

Sira Sriswasdi, Sandra L Harper, Hsin-Yao Tang, David W Speicher

Abstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Sira SriswasdiCenter for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute , 3601 Spruce Street, Philadelphia, Pennsylvania 19104, United States.
Sandra L Harper
Hsin-Yao Tang
David W Speicher

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
CHANGES IN THE RBC PROTEOME DURING HEALTH AND DISEASER01DK084188 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI ABDULMALIK, OSHEIZA Y · 2010 to 2014
$2.0M
NCI NIH HHS P30 CA010815NCI NIH HHS P30CA010815NHLBI NIH HHS R01 HL038794NHLBI NIH HHS R01HL038794NIDDK NIH HHS R01 DK084188
6 · The paper itself

Abstract

Chemical cross-linking coupled to mass spectrometry provides structural information that is useful for probing protein conformations and providing experimental support for molecular models. "Zero-length" cross-links have greater value for these applications than longer cross-links because they provide more stringent distance constraints. However, this method is less commonly utilized because it cannot take advantage of isotopic labels, MS-labile bonds, or enrichment tags to facilitate identification. In this study, we combined label-free precursor ion quantitation and targeted tandem mass spectrometry with a new software tool, Zero-length Cross-link Miner (ZXMiner), to form a multitiered analysis strategy. A major, critical objective was to simultaneously achieve very high accuracy with essentially no false-positive cross-link identifications while maintaining a good depth of analysis. Our strategy was optimized on several proteins with known crystal structures. Comparison of ZXMiner to several existing cross-link analysis software showed that other algorithms detected less true positive cross-links and were far less accurate. Although prior use of zero-length cross-linking was typically restricted to small proteins, ZXMiner and the associated strategy enable facile analysis of very large protein complexes. This was demonstrated by identification of zero-length cross-links using purified 526 kDa spectrin heterodimers and intact red cell membranes and membrane skeletons.

Indexed as

Chromatography, LiquidCross-Linking ReagentsErythrocyte MembraneGlutathione TransferaseHumansMyoglobinProtein ConformationTandem Mass SpectrometryCross-Linking ReagentsGlutathione TransferaseMyoglobin

Identifiers

PMID24369724
PMCPMC3975668

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.